T
Tong Sun Kobilka
Researcher at Stanford University
Publications - 31
Citations - 18245
Tong Sun Kobilka is an academic researcher from Stanford University. The author has contributed to research in topics: G protein-coupled receptor & Receptor. The author has an hindex of 22, co-authored 30 publications receiving 16810 citations. Previous affiliations of Tong Sun Kobilka include Howard Hughes Medical Institute.
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Journal ArticleDOI
High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor
Vadim Cherezov,Daniel M. Rosenbaum,Michael A. Hanson,Søren G. F. Rasmussen,Foon Sun Thian,Tong Sun Kobilka,Hee Jung Choi,Peter Kuhn,William I. Weis,Brian K. Kobilka,Raymond C. Stevens +10 more
TL;DR: Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.
Journal ArticleDOI
Crystal structure of the β2 adrenergic receptor-Gs protein complex.
Søren G. F. Rasmussen,Brian T. DeVree,Yaozhong Zou,Andrew C. Kruse,Ka Young Chung,Tong Sun Kobilka,Foon Sun Thian,Pil Seok Chae,Els Pardon,Els Pardon,Diane M. Calinski,Jesper Mosolff Mathiesen,Syed T. A. Shah,Joseph A. Lyons,Martin Caffrey,Samuel H. Gellman,Jan Steyaert,Jan Steyaert,Georgios Skiniotis,William I. Weis,Roger K. Sunahara,Brian K. Kobilka +21 more
TL;DR: This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.
Journal ArticleDOI
Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.
Søren G. F. Rasmussen,Hee Jung Choi,Daniel M. Rosenbaum,Tong Sun Kobilka,Foon Sun Thian,Patricia C. Edwards,Manfred Burghammer,Venkata R. P. Ratnala,Ruslan Sanishvili,Robert F. Fischetti,Gebhard F. X. Schertler,William I. Weis,Brian K. Kobilka +12 more
TL;DR: In this paper, the human beta2 adrenoceptor (beta2AR) was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop.
Journal ArticleDOI
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Søren G. F. Rasmussen,Hee Jung Choi,Juan Jose Fung,Els Pardon,Paola Casarosa,Pil Seok Chae,Brian T. DeVree,Daniel M. Rosenbaum,Foon Sun Thian,Tong Sun Kobilka,Andreas Schnapp,Ingo Konetzki,Roger K. Sunahara,Samuel H. Gellman,Alexander Pautsch,Jan Steyaert,William I. Weis,Brian K. Kobilka +17 more
TL;DR: A camelid antibody fragment to the human β2 adrenergic receptor is generated, and an agonist-bound, active-state crystal structure of the receptor-nanobody complex is obtained, providing insights into the process of agonist binding and activation.
Journal ArticleDOI
GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function
Daniel M. Rosenbaum,Vadim Cherezov,Michael A. Hanson,Søren G. F. Rasmussen,Foon Sun Thian,Tong Sun Kobilka,Hee Jung Choi,Xiao-Jie Yao,William I. Weis,Raymond C. Stevens,Brian K. Kobilka +10 more
TL;DR: Analysis of adrenergic receptor ligand-binding mutants within the context of the reported high-resolution structure of β2AR-T4L provides insights into inverse-agonist binding and the structural changes required to accommodate catecholamine agonists.